Archaeologists say they may have discovered one of the earliest examples of a 'crayon' -- possibly used by our ancestors 10,000 years ago for applying colour to their animal skins or for artwork.
The ochre crayon was discovered near an ancient lake, now blanketed in peat, near Scarborough, North Yorkshire. An ochre pebble was found at another site on the opposite side of the lake.
The pebble had a heavily striated surface that is likely to have been scraped to produce a red pigment powder. The crayon measures 22mm long and 7mm wide.
Ochre is an important mineral pigment used by prehistoric hunter-gatherers across the globe. The latest finds suggest people collected ochre and processed it in different ways during the Mesolithic period.
The ochre objects were studied as part of an interdisciplinary collaboration between the Departments of Archaeology and Physics at the University of York, using state-of-the-art techniques to establish their composition.
The artefacts were found at Seamer Carr and Flixton School House. Both sites are situated in a landscape rich in prehistory, including one of the most famous Mesolithic sites in Europe, Star Carr.
A pendant was discovered at Star Carr in 2015 and is the earliest known Mesolithic art in Britain. Here, more than 30 red deer antler headdresses were found which may have been used as a disguise in hunting, or during ritual performances by shamans when communicating with animal spirits.
Lead author, Dr Andy Needham from the University of York's Department of Archaeology, said the latest discoveries helped further our understanding of Mesolithic life.
He commented: "Colour was a very significant part of hunter-gatherer life and ochre gives you a very vibrant red colour. It is very important in the Mesolithic period and seems to be used in a number of ways.
"One of the latest objects we have found looks exactly like a crayon; the tip is faceted and has gone from a rounded end to a really sharpened end, suggesting it has been used.
"For me it is a very significant object and helps us build a bigger picture of what life was like in the area; it suggests it would have been a very colourful place."
The research team say Flixton was a key location in the Mesolithic period and the two objects help paint a vibrant picture of how the people interacted with the local environment.
"The pebble and crayon were located in an area already rich in art. It is possible there could have been an artistic use for these objects, perhaps for colouring animal skins or for use in decorative artwork," Dr Needham added.
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USC scientists have unlocked a new, more efficient pathway for converting methane -- a potent gas contributing to climate change -- directly into basic chemicals for manufacturing plastics, agrochemicals and pharmaceuticals.
In research published on Dec. 4 in the Journal of the American Chemical Society, chemists at USC Loker Hydrocarbon Research Institute say they have found a way to help to utilize this abundant and dangerous greenhouse gas, which is generally burnt or flared to produce energy.
Among common greenhouse gases, carbon dioxide is often cited as the largest culprit for trapping heat on earth, contributing to climate change. However, it is not the most potent.
That distinction belongs to methane. According to the Intergovernmental Panel on Climate Change, methane traps heat and warms the planet 86 times more than carbon dioxide over a 20-year horizon.
More fuel, fewer emissions, reduced energy use
Lead author Patrice T. D. Batamack, senior author G. K. Surya Prakash and Thomas Mathew of the USC Loker Hydrocarbon Research Institute used a catalyst called H-SAPO-34, derived from a class of nanoporous crystals called zeolites.
This simple method of converting methane directly to ethylene and propylene, or olefins, would replace what are traditionally difficult, expensive, and inefficient processes that add greenhouse gases to the atmosphere. The majority of ethylene and propylene is produced from petroleum oil and shale liquid cracking, which consumes enormous amounts of energy.
When USC's first Nobel Prize winner, George Olah, converted methane to olefins in 1985, the process required three steps. Since then, researchers have reduced it to two steps, but the Loker team is the first to realize the conversion with a single catalyst based on zeolites.
"Contact time is the key for this effective and simple catalyst to produce usable fuel from methane. In real estate, they say, location, location, location. In chemistry, it is all about condition, condition, condition," said Prakash.
Global methane emissions have surged since 2007 and output is particularly bad in the United States. According to a recent Harvard University study, the United States could be solely responsible for as much as 60 percent of the global growth in human-caused atmospheric methane emissions during this century.
Contributing to the global surge is the increased supply of livestock and rice fields in countries like India and China, the two leaders in total methane output, according to the World Bank.
'If carbon is the problem, carbon has to be the solution'
While being the most potent of our popular greenhouse gases, and even after the largest methane leak in U.S. history at the Aliso Canyon natural gas storage facility a few years ago, there are no signs that methane's abundant production will slow down anytime soon.
Shale fracking and other resource extraction techniques are increasing natural gas reserves, and the Loker scientists believe methane may soon become the most popular of all raw materials for producing petrochemical products.
About 30 years ago, Prakash and his mentor Olah first began refining the concept of "The Methanol Economy," a host of methanol-based solutions mitigating the production cycle of the greenhouse gases that are accelerating climate change.
While similar in structure and name, methane is not directly interchangeable with methanol, although most methanol is synthetically produced from methane. Methane is a naturally occurring gas and the simplest one-carbon compound containing hydrocarbon.
By further reducing the steps necessary to efficiently convert methane to olefins, the scientists at Loker may have brought us that much closer to realizing one of the original steps laid out in "The Methanol Economy."
"If carbon is the problem, carbon has to be the solution. There is plenty of methane to go around in the world and it is become easier and safer to turn it into products that we can actually use,'" said Prakash.
This research was made possible with the support of the USC Loker Hydrocarbon Research Institute and the U.S. Department of Energy.
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Picture a tiny, makeshift muscle that can curl a 20 milligram suspended weight when exposed to light. Under the right conditions, another mix packs enough power to bench-press a dime.
Researchers at Washington University in St. Louis have created a completely new kind of artificial molecular muscle from a polymer that's capable of some heavy lifting -- relatively speaking.
"The external trigger that initiates the actuation process can be something as simple as sunlight," said Jonathan Barnes, assistant professor of chemistry in Arts & Sciences and a 2017 Packard Fellow. The novel polymer, which changes color and contracts when exposed to visible light, is described in a Jan. 24 publication of a special issue of Macromolecular Rapid Communications.
Barnes and his team have been working on their proof of concept for the novel redox-responsive polymer -- one that contracts when electrons are added (reduction) and expands when they are taken away (oxidation) -- since he started at Washington University less than two years ago.
Last fall, they demonstrated that they could successfully build their functional polymer and incorporate it into a pliant, bulk material called a hydrogel. The resulting material could be contracted to one-tenth its original volume and then expanded back to its original size, its long polymer chains delicately folding and unfolding in three dimensions.
The hydrogel contains 5 percent polymer overall, of which only 5 percent is the new, functional polymer; the rest is just water. This means that only 0.25 percent of the total hydrogel is the functional polymer, an incredibly low number in the field.
"If you look at other materials, the active polymer is usually in every link," said Angelique Greene, a postdoctoral fellow in the Barnes laboratory. "Ours is very dilute, and yet our hydrogels still performed at a comparable and sometimes even better rate."
Pulling their own weight
But the molecular muscle still needed to be triggered by chemical reduction in a wet solution. To address the slosh factor, the researchers then introduced visible-light-absorbing photoredox catalysts, embedded in the gel, and moved their muscles onto dry ground.
It was time for a strength test.
"We wanted to demonstrate that it could not only change shape, or bend, or turn a different color, but actually do work," Barnes said.
The researchers affixed their best-performing gel to a piece of black electrical tape, and then attached a small, light piece of aluminum wire holding a small 20 milligram weight on the bottom. They exposed it to a blue light, and, after five hours, the polymer had moved the suspended weight several centimeters from its starting position.
"Here we have a lot fine control," said Kevin Liles, a PhD candidate in chemistry who co-wrote the new study, along with Greene. "We can irradiate the polymer for a certain amount of time, stop it at a certain number of degrees (of bend), or irradiate a certain portion and get it to contract in certain areas."
Five hours might seem like a long time to move a few centimeters, but Barnes isn't worried that Mother Nature does it faster.
"If you've ever seen a flower or plant on the side of a mountain, it always bends toward where the light is," Barnes said. "Nature finds a way to adapt to optimize the amount of light source that hits its petals. This material in principle does the exact same thing."
The researchers are now looking at how to pair their novel functional polymer with others that are tougher and capable of lifting heavier loads. They also want to figure out how to control the artificial molecular muscles using electrodes. This action would be similar to the way that electrical signals are transmitted in the body, and could pave the way toward future prosthetic applications.
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Scales are the material of choice for animals from pangolins to fish: They're customizable, water-friendly, strong but flexible, and easy to fix when damaged.
Scientists would like to recreate this unique structure -- they can imagine uses from medical implants to flexible electronics -- but it's proved difficult using non-organic materials. But researchers with the University of Chicago have published a concept to use a naturally occurring mineral called calcite to "grow" scales that can attach to soft materials. The setup could one day serve as waterproof implants to reinforce bones or joints.
Currently surgeons use structures made out of synthetic polymers, but while they're easy to sculpt, they can degrade over time. For a replacement, the UChicago team instead started with two materials that are compatible with the body.
Silicone is a flexible, rubbery material often used in surgical implants because it doesn't react with human tissue. Calcite is a common hard mineral that many clams and oysters use in their shells (brittlestars, related to starfish, use calcite in their eyes, as did ancient trilobites). Luckily, one of the specialties of Asst. Prof. Bozhi Tian's chemistry lab is combining hard and soft materials at the molecular level.
In a paper published last fall in Nature Communications, Tian and collaborators designed a system of minuscule two-ended hooks, made out of calcite, that can "grow" from silicone into tissue to fix themselves into place.
"Silicone alone won't immobilize tissue components, and calcite alone is too stiff, but the combination of the two works very well," Tian said. "The result is a structure that is both strong and flexible."
The tiny structures, each about the size of a red blood cell, are shaped like dumbbells. One end hooks into the silicone; the other protrudes above the surface. The team tried laying a strip of lab-grown tissue on top. The dumbbells picked up calcium from the cells and grew into the tissue, affixing themselves in place.
One nice feature is that the implant could be crafted with "hooks" only in very specific places. "This method is particularly useful for biological adhesion, where you want to apply your glue very sparingly to avoid interfering in the body more than necessary," said Jaeseok Yi, a postdoctoral scholar and the first author of this paper.
The research used X-rays and facilities at the Advanced Photon Source and the Center for Nanoscale Materials at Argonne National Laboratory.
Other UChicago co-authors were Yuanwen Jiang and Ivo Peters. Other authors came from Argonne, the University of Science and Technology of China, the University of Southampton in the UK and Hanyang University in South Korea.
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Chemists have measured the effects of nanoconfinement in catalysis by tracking single molecules as they dive down "nanowells" and react with catalysts at the bottom.
The wells in these experiments are just an average 2.3 billionths of a meter wide and about 80 to 120 billionths of a meter deep. These tiny channels provide access to a platinum catalyst sandwiched between the solid cores and porous shells of silica spheres. And they're helping a team of chemists understand how such nanoconfinement of catalysts affects reactions.
Previous studies of the reactions have been limited to theoretical work with simplified models and experiments following a collection of molecules. This study was able to collect single-molecule data because the experiment created a fluorescent molecule that could be lit, imaged and tracked -- even in nanoconfinement.
"This nanoconfinement effect is not well understood, especially at a quantitative level," said Wenyu Huang, an Iowa State University associate professor of chemistry and an associate of the U.S. Department of Energy's Ames Laboratory.
A new paper recently published online by the journal Nature Catalysis reports that, in this case, "the reaction rate is significantly increased in the presence of nanoconfinement," wrote Huang and a team of co-authors.
Huang and Ning Fang, an associate professor of chemistry at Georgia State University in Atlanta, are lead authors of the paper. A three-year, $550,000 grant from the National Science Foundation supported the project.
Huang's Iowa State lab created, studied and described the multi-layered spheres and their nanowells of prescribed length. Fang's lab at Georgia State used laser and microscopic imaging technology to track the molecules and measure the reactions.
That was a major challenge for the researchers. Such measurements had never been taken experimentally "due to the seemingly insurmountable technical challenges of tracking single molecules dynamically in complex nanoporous structures under reaction conditions," the chemists wrote in their paper.
They, however, devised an experimental technique that successfully tracked more than 10,000 molecule trajectories of a model catalytic reaction. (The reaction involved a molecule called amplex red reacting with hydrogen peroxide on the surface of platinum nanoparticles to generate a product molecule called resorufin, which is a highly fluorescent molecule.)
In addition to finding that nanoconfinement increased the reaction rate, the experiments showed there was less adhesion of the molecules to the surface of the platinum nanoparticles.
Now that they have demonstrated their experimental techniques and made initial conclusions, the chemists plan to expand their project.
"Once we understand this model, we can look at more complicated reactions," Huang said.
And that could lead to better catalysts.
As the chemists wrote in their paper, "This work paves the way for research to quantitatively differentiate, evaluate and understand the complex nanoconfinement effects on dynamic catalytic processes, thus guiding the rational design of high-performance catalysts."
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A team of chemical and biological engineers has developed highly selective membrane filters that could enable manufacturers to separate and purify chemicals in ways that are currently impossible, allowing them to potentially use less energy and cut carbon emissions, according to findings published in print today in the journal ACS Nano.
Tufts University scientists said the sophisticated membranes can separate organic compounds not only by size -- as small as a molecule -- but also by their electrostatic charge, meaning manufacturers could sort compounds by both size and type. The membranes use a simple, scalable process in which a specialty polymer is dissolved in a solvent and coated onto a porous support. The polymer self-assembles to create approximately 1 nanometer size channels that mimic biological systems, such as ion channels, which control the passage of compounds through cell membranes with great effectiveness.
Corresponding-author Ayse Asatekin, Ph.D., a chemical and biological engineering professor in the Tufts School of Engineering, said the team's discovery responds to industry-wide calls for the development of more efficient solutions for separating chemicals, which accounts for 10 to 15 percent of global energy use, according to a report in Nature.
"Our study is promising because it is the first demonstration of a new way of making these selective membranes that are so important for chemical manufacturing," she said. "Designing very selective membranes that can perform these complex separations could really boost energy efficiency and greatly reduce manufacturing waste."
The newly designed membranes can:
-- Allow neutral compounds to pass through 250 times faster than charged compounds of similar size;
-- When charged and uncharged compounds are mixed, prevent the charged compound from passing through at all -- its passage is averted because the neutral compound gets into the channels first and prevents the charge compound from entering; and
-- Provide the ability to separate charged and uncharged compounds in various filtration systems.
Asatekin noted that the charge-based separation is enhanced when the solution contains a mixture of solutes, which indicates that the membrane structure successfully mimics how biological systems such as ion channels operate. This discovery has led the researchers to believe that this approach can be used to address other separations, and bring about selectivities above and beyond what can be attained using conventional membranes.
"This means we could potentially make filters that are capable of separations that cannot be achieved currently. Filters today usually are limited to separating big from small, and we want to be able to separate compounds that are the same size but different," Asatekin said.
Asatekin noted some potential applications for this project include the purification of antibiotics, amino acids, antioxidants and other small molecule biologic compounds, and the separation of ionic liquids from sugar in biorefinery facilities. However, she said she believes this general approach may potentially be adapted further to different separations with further research.
Asatekin serves as the principal investigator of the Smart Polymers, Membranes, and Separations Laboratory at Tufts. The lab aims to develop the next generation of membranes by designing them from molecules up. The membranes rely on polymers that self-assemble, form nanostructures, and expose chemical functionalities that enable them to perform tasks normally not expected from membranes. They remove not only bacteria but also heavy metals, react to stimuli, and separate small molecules by chemical structure. Overall, the goal is to develop membranes that will help generate clean, safe water more efficiently and separate chemicals with lower energy use.
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Rutgers scientists have found the "Legos of life" -- four core chemical structures that can be stacked together to build the myriad proteins inside every organism -- after smashing and dissecting nearly 10,000 proteins to understand their component parts.
The four building blocks make energy available for humans and all other living organisms, according to a study published online today in the Proceedings of the National Academy of Sciences.
The study's findings could lead to applications of these stackable, organic building blocks for biomedical engineering and therapeutic proteins and the development of safer, more efficient industrial and energy catalysts -- proteins and enzymes that, like tireless robots, can repeatedly carry out chemical reactions and transfer energy to perform tasks.
"Understanding these parts and how they are connected to each other within the existing proteins could help us understand how to design new catalysts that could potentially split water, fix nitrogen or do other things that are really important for society," said Paul G. Falkowski, study co-author and a distinguished professor who leads the Environmental Biophysics and Molecular Ecology Laboratory at Rutgers University-New Brunswick.
The scientists' research was done on computers, using data on the 3D atomic structures of 9,500 proteins in the RCSB Protein Data Bank based at Rutgers, a rich source of information about how proteins work and evolve.
"We don't have a fossil record of what proteins looked like 4 billion years ago, so we have to take what we have today and start walking backwards, trying to imagine what these proteins looked like," said Vikas Nanda, senior author of the study and an associate professor in the Department of Biochemistry and Molecular Biology at Rutgers' Robert Wood Johnson Medical School, within Rutgers Biomedical and Health Sciences. "The study is the first time we've been able to take something with thousands of amino acids and break it down into reasonable chunks that could have had primordial origins."
The identification of four fundamental building blocks for all proteins is just a beginning. Nanda said future research may discover five or 10 more building blocks that serve as biological Legos.
"Now we need to understand how to put these parts together to make more interesting functional molecules," he said. "That's the next grand challenge."
The study's lead author is Hagai Raanana, a post-doctoral associate in the Environmental Biophysics and Molecular Ecology Program. Co-authors include Douglas H. Pike, a doctoral student at the Rutgers Institute for Quantitative Biomedicine, and Eli K. Moore, a post-doctoral associate in the Environmental Biophysics and Molecular Ecology Program.
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New insight into science that seems, on its surface, exceedingly simple -- what happens when you add salt to water -- could ultimately lead to a better understanding of biochemical processes in cells and perhaps advance sources of clean energy.
An article published in the Journal of Physical Chemistry Letters on that topic earlier in 2017 has generated considerable interest, according to the journal's editors. The article was written by Giulia Galli, a Liew Family Professor in Molecular Engineering at the University of Chicago who has a joint appointment at the U.S. Department of Energy's (DOE) Argonne National Laboratory, and Alex Gaiduk, a Natural Sciences and Engineering Research Council of Canada postdoctoral fellow at the University of Chicago.
"Scientists can now perhaps develop new computational models to describe biochemical processes in cells, and this could lead to the development of new drugs." -- Alex Gaiduk, Natural Sciences and Engineering Research Council of Canada postdoctoral fellow at the University of Chicago
"One of the questions that has puzzled researchers for decades is how far ions affect the structure of saline water, the same kind of solutions that are present in our bodies," said Gaiduk, a chemist and theorist. One popular view is that ions have a local effect on the structure of water, causing hydrogen bonds to form or break only close to the ion. But it seems that isn't always the case.
"The reason this problem was still open is that experiments do not provide direct detailed information about the structure of the liquid at the molecular level," Gaiduk said. "Instead, they provide averaged information coming from the entire molecular system, which is often hard to interpret."
Meanwhile, molecular simulations provide first-hand information about the molecular structure of the liquid and can shed light on the ions' influence on the water structure. Determined to answer these questions, Gaiduk and Galli turned to the Argonne Leadership Computing Facility (ALCF), a DOE Office of Science User Facility capable of carrying out simulations that require massive computational capabilities -- 10 to 100 times more powerful than those of systems typically used for scientific research.
Gaiduk and Galli used the ALCF to simulate sodium chloride in water, and gathered extensive amounts of data. They analyzed the results and discovered that the sodium ion indeed has only a local effect on water structure, while the chlorine ion has a farther-reaching effect, modifying the water structure at least up to a nanometer away from the ion. (A nanometer is one-billionth of a meter.)
"We have provided important information about the structure of water in the presence of dissolved salts -- namely that some ions, including chloride, have a long-range effect while others, such as sodium, do not," Gaiduk said. "We used non-empirical simulation methods and a rather sophisticated choice of molecular signatures of the water structure."
The research provides a new fundamental understanding of sodium chloride in water. This is one of the aqueous systems used in photoelectrochemical cells. These cells are used to split water into hydrogen and oxygen, a technology that has long-term potential as a clean energy source. Additional research will be required to determine how this new understanding might be used to improve the technology, Galli said.
Their finding could also prove valuable for biochemistry on a number of fronts.
"Processes like protein folding, crystallization and solubility are at the core of all biological and biochemical processes that essentially define life," said Gaiduk, adding that this finding may contribute to explaining the solubility of proteins. "Scientists can now perhaps develop new computational models to describe biochemical processes in cells, and this could lead to the development of new drugs."
However, the authors concluded that the subtle modifications of the structure of water by the ions -- even chlorine -- are probably insufficient to explain the different solubility of biomolecules in pure and salty water. Clearly researchers have more work to do before they can fully understand and model interactions of ions with the functional groups of proteins. However, this technique for analyzing the hydrogen bond network of water is a first step to help scientists understand how the structure of water changes with the addition of salt.
Using the results obtained by Gaiduk and Galli, another research group has developed a new model that correctly describes the effect of ions on the structure of water. Their findings are detailed in the Aug. 31, 2017 issue of the Journal of Physical Chemistry B.
Funding for the work by Gaiduk and Galli was provided by DOE's Office of Science, Basic Energy Sciences, through the Midwest Integrated Center for Computational Materials and the Natural Sciences and Engineering Research Council of Canada. Computer time was provided by the Innovative and Novel Computational Impact on Theory and Experiment (INCITE) program.
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The human body has two primary kinds of fat -- white fat, which stores excess calories and is associated with obesity, and brown fat, which burns calories in order to produce heat and has garnered interest as a potential means of combating obesity.
Now, a study led by Brown University researchers has identified an enzyme that appears the regulate the physiology of both fat types in mice -- decreasing inflammation in white fat tissue, while promoting the ability of brown fat to burn calories. Preliminary genetic evidence included in the study suggests that the enzyme, called SNRK, performs similar functions in humans, making it an intriguing new drug target in the battle against obesity and its complications.
"This study suggests that there may be dual benefits if we can find a way to enhance SNRK production in fat tissue," said Simin Liu, a study co-corresponding author and professor of epidemiology in Brown's School of Public Health and professor of medicine at the Alpert School of Medicine. "Reducing inflammation in white fat may ease associated complications such as insulin resistance, while at the same time, increasing brown fat metabolism may aid in weight loss. Those possibilities will need to be followed up in further studies in humans."
The research, published in the journal Diabetes, was led by Jie Li, a research associate in epidemiology at Brown, and Bin Feng, a research associate at the Warren Alpert Medical School of Brown University and Rhode Island Hospital's Hallett Center for Diabetes and Endocrinology.
The presence of SNRK in fat tissue was first discovered by co-corresponding author Haiyan Xu while she was a researcher in the Molecular Epidemiology and Nutrition Lab of Brown's Center for Global Cardiometabolic Health. Her initial research suggested that the enzyme played a role in regulating inflammation, but this latest study was designed to get a more complete picture of its function in fat tissue.
Inflammation and metabolism
For this new study, the researchers bred mice that lack the gene for producing SNRK in fat cells. They could then compare fat tissue from those mice with tissue from normal mice.
The study showed that mice lacking the SNRK gene had a significantly higher concentration of macrophages in white fat tissue compared with normal mice. Macrophages are immune cells commonly used as markers for inflammation, and their increased presence helps confirm that SNRK plays a role in regulating inflammation in white fat tissue.
It's an intriguing finding, Xu says, because her previous research has shown that inflammation in white fat is associated with insulin resistance, a risk factor for the development of diabetes.
In addition to its effects on white fat, the researchers showed that SNRK influences the physiology of brown fat tissue. Mice lacking the SNRK gene tended to be heavier than normal mice, and were shown to have lower overall metabolic rates. The SNRK-lacking mice maintained their extra weight even when treated with a drug known to induce weight loss in rodents by activating brown fat. That suggests that the lower metabolic rate and extra weight carried by the mice lacking the SNRK gene was due in part to reduced brown fat metabolism.
"What that tells us is that boosting SNRK production might have the effect of boosting overall metabolism, which might aid in weight loss," Xu said.
Function in humans
Having established that SNRK appears to regulate fat tissue inflammation and metabolism in mice, the researchers took a step further investigating whether SNRK may play a similar role in humans. The team identified multiple germline mutations in the human genes responsible for SNRK production that were directly associated with higher body mass index, higher waist circumference and risk of obesity in a cohort of 12,000 women who participated in the Women's Health Initiative.
Taken together, the researchers say, the results suggest that SNRK could be a target for new therapies aimed at curbing obesity and its complications.
"What's particularly noteworthy about this work is we were able to present an integrative link from genetics, cell- and animal-based experiments, all the way up to clinical outcomes in large human population," Liu said. "We hope that making that connection will quicken the process of multidisciplinary collaborations in translating lab-based discoveries to new therapies or targets for interventions."
Additional authors on the study were Yaohui Nie, Ping Jiao, Xiaochen Lin, Mengna Huang, Ran An, Qin He, Huilin Emily Zhou, Arthur Salomon, Kirsten S Sigrist and Zhidan Wu. The research was supported by the National Institutes of Health (R01 DK103699, HHSN268201100003, NIGMS 8P30 GM103410), the American Heart Association and the National Science Foundation (1557467 QuBBD).
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Although antipsychotic drugs are among the most widely prescribed medications, individuals with schizophrenia, bipolar disorder and autism-spectrum disorders often experience severe side effects because the drugs interact with dozens of other brain receptors. Now, scientists at the UNC School of Medicine and UC San Francisco (UCSF) have solved the first high-resolution crystal structure of the dopamine 2 receptor (DRD2) bound to the antipsychotic drug risperidone, yielding a long-awaited tool for drug developers, psychiatrists, and neuroscientists.
The research, published in Nature, will allow researchers to selectively activate DRD2 thus potentially limiting a host of serious antipsychotic drug side effects such as weight gain, anxiety, dizziness, severe digestive problems, agitation, and many others.
"If we want to create better medications, the first step is to see what the D2 receptor looks like in high-resolution detail when it's bound tightly to a drug," said senior author Bryan L. Roth, MD, PhD, the Michael Hooker Distinguished Professor of Protein Therapeutics and Translational Proteomics at the UNC School of Medicine. "We now have the structure, and we're exploring it to find new compounds we hope can help the millions of people in need of better treatments."
About 30 percent of medications on the market activate G-protein coupled receptors on cell surfaces and trigger chemical signals inside cells to yield their therapeutic effects. For antipsychotic medications, one effect is alleviating psychotic symptoms associated with schizophrenia, bipolar disorder and many other psychiatric diseases. Unfortunately, because scientists haven't understood the structural differences between the many different kinds of receptors in the brain, most drugs cannot be designed to target only one type of receptor; they interact with not only DRD2, but a myriad of other dopamine, serotonin, histamine, and alpha adrenergic receptors, leading to serious side effects.
DRD2 has undergone extensive study for 30 years, but until now researchers lacked a high-resolution structure of DRD2 attached to a compound. Risperidone is a commonly prescribed antipsychotic medication which is FDA approved for use for schizophrenia, bipolar disorder, and autism spectrum disorder. Risperidone is also one of the very few 'atypical' antipsychotic drugs approved for use in children.
"With this high-resolution structure in hand, we anticipate the discovery of compounds that interact with DRD2 in specific ways important for greater therapeutic actions and fewer side-effects," Roth said.
Typically scientists have solved the chemical structure of proteins using a technique called X-Ray crystallography. They use experimental approaches to induce the protein to condense into a tightly packed crystal lattice, then shoot x-rays at the crystal, and finally calculate the protein's structure from the resulting diffraction patterns. However, getting the DRD2 protein to crystalize with a drug bound to it had been impossible for decades because receptors are notoriously fickle proteins -- small, fragile, and typically in motion as they bind to compounds.
To transcend the technical challenges, Roth and UNC colleagues, including postdoctoral fellows Sheng Wang, PhD, and Daniel Wacker, PhD, conducted a series of painstaking studies over several years -- outlined in the Nature paper -- to coax DRD2 to crystalize while bound tightly to risperidone.
Once they had the high-resolution image, they could see that risperidone binds to DRD2 in an entirely unexpected way. Further computational modeling performed by UCSF researchers Brian Shoichet, PhD, and Anat Levit, PhD, revealed that risperidone's binding mode was unpredictable -- there was a previously unseen pocket on the receptor which Roth and colleagues think could be targeted to create more selective medications.
"Now that we can see the structural differences between similar receptors, such as the dopamine D4 receptor and DRD2, we can envision new methods for creating compounds that only bind to DRD2 without interacting with dozens of other brain receptors." said Wacker, co-corresponding author of the study. "This is precisely the sort of information we need in order to create safer and more effective therapeutics."
Adverse effects of antipsychotic drugs include extrapyramidal symptoms, such as Parkinsonian involuntary muscle movement. Wang said, "Now that we've solved the structure of risperidone bound to DRD2, we are getting an idea how these side effects could be avoided."
Roth added, "Before coming to UNC, I was a psychiatrist specializing in treating schizophrenia. On a daily basis it was clear to me that medications were only modestly effective for large numbers of patients. Our lack of knowledge into how antipsychotic drugs bind to their receptors has held back progress towards creating more effective medications. Solving the high-resolution crystal structure of DRD2 bound to the commonly prescribed antipsychotic drug risperidone is the first step towards the creation of safer and more effective medications for schizophrenia and related disorders."
The National Institutes of Health funded this research. UNC School of Medicine postdoc Tao Che, PhD, was also a study author.
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First, as for the global residential Brass Rods industry, the industry concentration rate is highly dispersed. The top 5 manufacturers have 30.61% sales revenue market share in 2017. The Wieland which has 7.62% sales market share in 2017, is the leader in the Brass Rods industry. The manufacturers following Wieland are Daechang and KME, which respectively has 6.51% and 6.46% sales market share globally.
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Global Brass Rods Market by Manufacturers, Countries, Type and Application, Forecast to 2022
Global (North America, Europe and Asia-Pacific, South America, Middle East and Africa) Brass Rods Market 2017 Forecast to 2022
Second, the global consumption of Brass Rods products rises up from 2380 K Ton in 2012 to 2840 K Ton in 2017, with CAGR of 4.52%. At the same time, the revenue of world Brass Rods sales market has a rise from 11807.52 M USD to 13683.32 M USD. The reason causes this increase is the growing demand for the Brass Rods products, which is the result of the spurring needs of downstream customers, especially for Automobile.
Third, as for the Brass Rods market, it will still show slow growth, and technological trends in the market will stay stable.
Fourth, market growth for Brass Rods is expected to growth at a CAGR of 3.17% from 2017 to 2022, reaching 16567.95 M USD by 2022.
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